Adsorption of albumin on prosthetic materials: implication for tribological behavior.

Adsorption of albumin on prosthetic materials: implication for tribological behavior.
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DOI:
10.1002/jbm.a.30754
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发表时间:
2006-09
期刊:
Journal of biomedical materials research. Part A
影响因子:
--
通讯作者:
A. P. Serro;M. Gispert;M. Martins;P. Brogueira;R. Colaço;B. Saramago
A. P. Serro;M. Gispert;M. Martins;P. Brogueira;R. Colaço;B. Saramago
中科院分区:
其他
文献类型:
--
作者:
A. P. Serro;M. Gispert;M. Martins;P. Brogueira;R. Colaço;B. Saramago

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用于替代受损的自然关节的矫形假体由一种含有潜在边界润滑性能的生物大分子的假滑液进行润滑。蛋白质是其中的一些大分子,其在润滑过程中的作用还没有完全被了解。在以前的工作中,我们研究了主要滑膜蛋白白蛋白的存在对三种最常用的人工关节材料的摩擦学行为的影响:超高相对分子质量聚乙烯(UHMWPE)与氧化铝、CoCrMo合金和316L不锈钢的对接。当表面为金属时,由于避免了UHMWPE的转移,白蛋白导致摩擦系数显著降低,但对于氧化铝,这种影响要弱得多。本研究的目的是从白蛋白吸附的角度来解释摩擦学行为的这些差异。以此为目标,利用放射性标记白蛋白(~(125)I-BSA)、X射线光电子能谱和原子力显微镜研究了牛血清白蛋白(BSA)在生物模型流体(Hanks平衡盐溶液)表面材料上的吸附。所有技术的结论是,白蛋白在金属表面的吸附驱动力比在氧化铝上的要大。这些结果证实,蛋白质吸附在表面上的量越大,保护聚合物膜向表面转移的效果就越好。
The orthopedic prosthesis used to substitute damaged natural joints are lubricated by a pseudosynovial fluid that contains biological macromolecules with potential boundary lubrication properties. Proteins are some of those macromolecules whose role in the lubrication process is not yet completely understood. In a previous work, we investigated the influence of the presence of albumin, the major synovial protein, upon the tribological behavior of three of the most used pairs of artificial joint materials: ultra high molecular weight polyethylene (UHMWPE) against counterfaces of alumina, CoCrMo alloy, and 316L stainless steel. Albumin was found to cause a significant decrease in the friction coefficient when the counterfaces were metallic because transfer of UHMWPE was avoided, but this effect was much weaker in the case of alumina. The objective of the present work was to look for an explanation for these differences in tribological behavior in terms of albumin adsorption. With this goal, studies on adsorption of bovine serum albumin (BSA) on the counterface materials, from a biological model fluid (Hanks' balanced salt solution), were carried out using radiolabeled albumin ((125)I-BSA), X-ray photoelectron spectroscopy, and atomic force microscopy. The conclusion from all techniques is that the driving force for albumin adsorption is higher on the metals than on alumina. These results confirm that the greater the amount of protein adsorbed on the counterface, the more efficient is the protection against the transfer of polymeric film to the counterface.